ArticleBiochemistry2007
Structure of the DNA-binding domain of the response regulator PhoP from Mycobacterium tuberculosis.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Serine/threonine protein kinase phosphorylation of DosR alters target gene transcription mechanics and regulates Mycobacterium tuberculosis response to nitric oxide stress.PLoS genetics · 2026Article
- The PhoPQ two-component regulatory system as an important regulator of bacterial stress response.Molecular biology reports · 2025Review
- ENcyclopedia of TRAnscription Factors in Bacteria and Archaea genomes (ENTRAF) version 2.0.Database : the journal of biological databases and curation · 2025Article
- The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.Molecular biomedicine · 2022Review
- Quantitative proteomics reveals that dormancy-related proteins mediate the attenuation in mycobacterium strains.Virulence · 2021Article
- Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states.Acta crystallographica. Section D, Structural biology · 2021Article
- Genome-Based Drug Target Identification in Human PathogenFrontiers in genetics · 2021Article
- A Low-Prevalence Single-Nucleotide Polymorphism in the Sensor Kinase PhoR inFrontiers in microbiology · 2021Article
- Interplay of PhoP and DevR response regulators defines expression of the dormancy regulon in virulentThe Journal of biological chemistry · 2018Article
- The Structure of the Biofilm-controlling Response Regulator BfmR from Acinetobacter baumannii Reveals Details of Its DNA-binding Mechanism.Journal of molecular biology · 2018Article
- Mycobacterial Dormancy Systems and Host Responses in Tuberculosis.Frontiers in immunology · 2017Review
- Structural basis of DNA sequence recognition by the response regulator PhoP in Mycobacterium tuberculosis.Scientific reports · 2016Article
- A High-Throughput Assay for Developing Inhibitors of PhoP, a Virulence Factor of Mycobacterium tuberculosis.Combinatorial chemistry & high throughput screening · 2016Article
- Structure of the Response Regulator NsrR from Streptococcus agalactiae, Which Is Involved in Lantibiotic Resistance.PloS one · 2016Article
- Solution structure of the PhoP DNA-binding domain from Mycobacterium tuberculosis.Journal of biomolecular NMR · 2015Article
- DNA consensus sequence motif for binding response regulator PhoP, a virulence regulator of Mycobacterium tuberculosis.Biochemistry · 2014Article
- Article
- Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae.Nucleic acids research · 2014Article
- Atypical response regulator ChxR from Chlamydia trachomatis is structurally poised for DNA binding.PloS one · 2014Article
- Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens.Virulence · 2014Review
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3 authors.
Funding
Abstract
The PhoP-PhoR two-component signaling system from Mycobacterium tuberculosis is essential for the virulence of the tubercle bacillus. The response regulator, PhoP, regulates expression of over 110 genes. In order to elucidate the regulatory mechanism of PhoP, we determined the crystal structure of its DNA-binding domain (PhoPC). PhoPC exhibits a typical fold of the winged helix-turn-helix subfamily of response regulators. The structure starts with a four-stranded antiparallel beta-sheet, followed by a three-helical bundle of alpha-helices, and then a C-terminal beta-hairpin, which together with a short beta-strand between the first and second helices forms a three-stranded antiparallel beta-sheet. Structural elements are packed through a hydrophobic core, with the first helix providing a scaffold for the rest of the domain to pack. The second and third helices and the long, flexible loop between them form the helix-turn-helix motif, with the third helix being the recognition helix. The C-terminal beta-hairpin turn forms the wing motif. The molecular surfaces around the recognition helix and the wing residues show strong positive electrostatic potential, consistent with their roles in DNA binding and nucleotide sequence recognition. The crystal packing of PhoPC gives a hexamer ring, with neighboring molecules interacting in a head-to-tail fashion. This packing interface suggests that PhoPC could bind DNA in a tandem association. However, this mode of DNA binding is likely to be nonspecific because the recognition helix is partially blocked and would be prevented from inserting into the major groove of DNA. Detailed structural analysis and implications with respect to DNA binding are discussed.
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